scholarly journals Response of leucine-rich repeat domain-containing protein in Haemaphysalis longicornis to Babesia microti infection and its ligand identification

2021 ◽  
Author(s):  
Jialing Yao ◽  
Zhengmao Xu ◽  
Zeyu Sun ◽  
Keke Zhou ◽  
Jinmiao Lu ◽  
...  
Keyword(s):  
Blood Feeding ◽  
Immunofluorescence Assay ◽  
Innate Immune ◽  
Babesia Microti ◽  
Hard Tick ◽  
Haemaphysalis Longicornis ◽  
Leucine Rich Repeat ◽  
Babesia Gibsoni ◽  
Leucine Rich Repeat Domain ◽  
Repeat Domain

Haemaphysalis longicornis is a blood-feeding hard tick known for transmitting a variety of pathogens, including Babesia. How the parasites in the imbibed blood become anchored in the midgut of ticks is still unknown. Leucine-rich repeat domain (LRR)-containing protein, which is associated with the innate immune reaction and conserved in many species, has been detected in H. longicornis and has previously been indicated in inhibiting the growth of Babesia gibsoni. However, the detailed mechanism is unknown. In this study, one of the ligands for LRR from H. longicornis (HlLRR) was identified in B. microti, designated as BmActin (Babesia microti actin), using GST pull-down experiments and immunofluorescence assay. Moreover, RNA interference of HlLRR led to a decrease in the BmActin mRNA expression in the midgut of fully engorged ticks, which fed on B. microti-infected mice. We also found that the expression level of the innate immune molecules in H. longicornis, defensin, antimicrobial peptides (AMPs), and lysozyme were downregulated after the knockdown of HlLRR. However, subolesin expression was upregulated. These results indicate that HlLRR not only recognizes BmActin but may also modulate innate immunity in ticks to influence Babesia growth, which will further benefit the development of anti-Babesia vaccines or drugs.

Identification of the Babesia-responsive leucine-rich repeat domain-containing protein from the hard tick Haemaphysalis longicornis

2015 ◽  
Vol 114 (5) ◽  
pp. 1793-1802 ◽  
Author(s):  
Hiroki Maeda ◽  
Koshi Kurisu ◽  
Takeshi Miyata ◽  
Kodai Kusakisako ◽  
Remil Linggatong Galay ◽  
...  
Keyword(s):  
Hard Tick ◽  
Haemaphysalis Longicornis ◽  
Leucine Rich Repeat ◽  
Leucine Rich Repeat Domain ◽  
Repeat Domain

Legumains from the hard tick Haemaphysalis longicornis play modulatory roles in blood feeding and gut cellular remodelling and impact on embryogenesis

2009 ◽  
Vol 39 (1) ◽  
pp. 97-107 ◽  
Author(s):  
M. Abdul Alim ◽  
Naotoshi Tsuji ◽  
Takeharu Miyoshi ◽  
M. Khyrul Islam ◽  
Takeshi Hatta ◽  
...  
Keyword(s):  
Blood Feeding ◽  
Hard Tick ◽  
Haemaphysalis Longicornis

scholarly journals SHOC2 subcellular shuttling requires the KEKE motif-rich region andN-terminal leucine-rich repeat domain and impacts on ERK signalling

2016 ◽  
Vol 25 (17) ◽  
pp. 3824-3835 ◽  
Author(s):  
Marialetizia Motta ◽  
Giovanni Chillemi ◽  
Valentina Fodale ◽  
Serena Cecchetti ◽  
Simona Coppola ◽  
...  
Keyword(s):  
Leucine Rich Repeat ◽  
Rich Region ◽  
Leucine Rich Repeat Domain ◽  
Repeat Domain

Valosin-containing protein from the hard tick Haemaphysalis longicornis: effects of dsRNA-mediated HlVCP gene silencing

2007 ◽  
Vol 85 (3) ◽  
pp. 384-394 ◽  
Author(s):  
Damdinsuren Boldbaatar ◽  
Badgar Battsetseg ◽  
Takeshi Hatta ◽  
Takeharu Miyoshi ◽  
Naotoshi Tsuji ◽  
...  
Keyword(s):  
Blood Feeding ◽  
Pcr Analysis ◽  
Hard Tick ◽  
Haemaphysalis Longicornis ◽  
Native Protein ◽  
Rt Pcr ◽  
Future Studies ◽  
Atpase Gene ◽  
A Domains

We report the cloning and characterization of a cDNA encoding the valosin-containing protein (VCP) from the Haemaphysalis longicornis tick (HlVCP). The full-length HlVCP is 2782 bp and codes for 808 amino acids of a deduced protein with a predicted molecular mass of 89.9 kDa. The domain structure analysis revealed that the deduced protein has 2 Walker A domains, 2 Walker B domains, a Cdc48 domain, and a polyQ-binding domain. The mouse anti-HlVCP serum recognized a 97 kDa native protein in the salivary glands, midgut, and synganglion. RT–PCR analysis revealed that the native VCP was expressed throughout the developing stages and in tick organs. HlVCP silencing resulted in a decrease in tick body mass after blood feeding. This study not only contributes to a growing understanding of the ATPase gene family but also lays the groundwork for future studies on protein secretion and host–tick interaction. This study is the first report of the VCP gene from Chelicerata, which include spiders, scorpions, and ticks.

scholarly journals NF-κB-Inducing Kinase Regulates Selected Gene Expression in the Nod2 Signaling Pathway

2006 ◽  
Vol 74 (4) ◽  
pp. 2121-2127 ◽  
Author(s):  
Qilin Pan ◽  
Vladimir Kravchenko ◽  
Alex Katz ◽  
Shuang Huang ◽  
Masayuki Ii ◽  
...  
Keyword(s):  
Host Defense ◽  
Innate Immune System ◽  
Muramyl Dipeptide ◽  
Innate Immune ◽  
Host Responses ◽  
Leucine Rich Repeat ◽  
Wild Type ◽  
Primary Explants ◽  
Repeat Domain

ABSTRACT The innate immune system surveys the extra- and intracellular environment for the presence of microbes. Among the intracellular sensors is a protein known as Nod2, a cytosolic protein containing a leucine-rich repeat domain. Nod2 is believed to play a role in determining host responses to invasive bacteria. A key element in upregulating host defense involves activation of the NF-κB pathway. It has been suggested through indirect studies that NF-κB-inducing kinase, or NIK, may be involved in Nod2 signaling. Here we have used macrophages derived from primary explants of bone marrow from wild-type mice and mice that either bear a mutation in NIK, rendering it inactive, or are derived from NIK−/− mice, in which the NIK gene has been deleted. We show that NIK binds to Nod2 and mediates induction of specific changes induced by the specific Nod2 activator, muramyl dipeptide, and that the role of NIK occurs in settings where both the Nod2 and TLR4 pathways are activated by their respective agonists. Specifically, we have linked NIK to the induction of the B-cell chemoattractant known as BLC and suggest that this chemokine may play a role in processes initiated by Nod2 activation that lead to improved host defense.

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